› 3hlk

X-ray diffraction
2.1Å resolution

Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2)

Released:
DOI: 10.2210/pdb3hlk/pdb
PDB entry 3hlk coloured by chain, front view.
PDB entry 3hlk coloured by chain, side view.
PDB entry 3hlk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2).
Mandel CR, Tweel B, Tong L
Biochem Biophys Res Commun 385 630-3 (2009)
PMID: 19497300

Function and Biology Details

Reaction catalysed: 
Palmitoyl-CoA + H(2)O = CoA + palmitate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156005 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl-coenzyme A thioesterase 2, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 446 amino acids
Theoretical weight: 49.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49753 (Residues: 46-483; Coverage: 91%)
Gene names: ACOT2, PTE2, PTE2A
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 16 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P3121
Unit cell:
a: 124.557Å b: 124.557Å c: 131.95Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.194 0.236
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Functional and structural properties of mammalian acyl-coenzyme A thioesterases.
Kirkby et al. (2010)
5 other articles

6 mentions without citation

Thioesterases: a new perspective based on their primary and tertiary structures.
Cantu et al. (2010)
5 more